|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
29-405 |
1.21e-166 |
|
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; Molybdopterin Mo-transferase (molybdopterin biosynthesis) is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440072 [Multi-domain] Cd Length: 401 Bit Score: 472.65 E-value: 1.21e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 29 TEQVATRRADGRVLAADVVAPIPLPAFDNSAMDGFAVRHADLSAAAPVTLELAGEQFAGPDLGLAVGPGQCVRITTGAPL 108
Cdd:COG0303 20 TETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVTLRVVGEIAAGSPPPGPLGPGEAVRIMTGAPL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 109 PSGADTIVIREDAIEQDGRVQVPAGIRAGAHVRRQGEDVATGDVVLRAGQVLTPARIGLAAALGIDRLEVAARPTVAVFA 188
Cdd:COG0303 100 PEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLLASLGIAEVPVYRRPRVAILS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 189 SGDELAEPGMPLRPGQVYNSNREQLMAQLRDAGLEPVAWPTLPDDPVLIAAVLDDAVENFDLVLTCGAVSAGEKDHLPRW 268
Cdd:COG0303 180 TGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEADLVITSGGVSVGDYDLVKEA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 269 LQARG-RIRFWKVRMRPGMPVLFGEAGRALVLGLPGNPVSVLATFHVFGRTLLDALQGRE--PRPCWRARLAAPWHKRHD 345
Cdd:COG0303 260 LEELGaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGLPppPPPRVRARLAEDLPKKPG 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 346 RLEFLRGRLDQDANaTLCVHPEPADGSHRLRAAASSDVLIVLEDGANAYVAGDVVEVLPL 405
Cdd:COG0303 340 RTEFLRVRLERDDG-ELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEVLLL 398
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
29-405 |
7.62e-159 |
|
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF), an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MoeA, together with MoaB, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes.
Pssm-ID: 238452 [Multi-domain] Cd Length: 394 Bit Score: 452.72 E-value: 7.62e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 29 TEQVATRRADGRVLAADVVAPIPLPAFDNSAMDGFAVRHADLsAAAPVTLELAGEQFAGPDLGLAVGPGQCVRITTGAPL 108
Cdd:cd00887 17 TETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADT-AGASVTLRVVGEIPAGEPPDGPLGPGEAVRIMTGAPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 109 PSGADTIVIREDAIEQDGRVQVPAGIRAGAHVRRQGEDVATGDVVLRAGQVLTPARIGLAAALGIDRLEVAARPTVAVFA 188
Cdd:cd00887 96 PEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAEVPVYRRPRVAIIS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 189 SGDELAEPGMPLRPGQVYNSNREQLMAQLRDAGLEPVAWPTLPDDPVLIAAVLDDAVENFDLVLTCGAVSAGEKDHLPR- 267
Cdd:cd00887 176 TGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGVSVGDYDFVKEv 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 268 WLQARGRIRFWKVRMRPGMPVLFGEAGRALVLGLPGNPVSVLATFHVFGRTLLDALQGRE--PRPCWRARLAAPWHKRHD 345
Cdd:cd00887 256 LEELGGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPepEPPRVKARLAEDLKSKPG 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 346 RLEFLRGRLDQDaNATLCVHPEPADGSHRLRAAASSDVLIVLEDGANAYVAGDVVEVLPL 405
Cdd:cd00887 336 RREFLRVRLERD-EGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLLL 394
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
29-405 |
1.41e-108 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 331.58 E-value: 1.41e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 29 TEQVATRRADGRVLAADVVAPIPLPAFDNSAMDGFAVRHADLSAA--APVTLELAGEQFAGPdlglaVGPGQCVRITTGA 106
Cdd:PRK14491 218 TEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPEsyTLVGEVLAGHQYDGT-----LQAGEAVRIMTGA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 107 PLPSGADTIVIREDAIEQDGRVQVPAGIRAGAHVRRQGEDVATGDVVLRAGQVLTPARIGLAAALGIDRLEVAARPTVAV 186
Cdd:PRK14491 293 PVPAGADTVVMRELATQDGDKVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPVFRRPKVAV 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 187 FASGDELAEPGMPLRPGQVYNSNREQLMAQLRDAGLEPVAWPTLPDDPVLIAAVLDDAVENFDLVLTCGAVSAGEKDHLP 266
Cdd:PRK14491 373 FSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISSGGVSVGDADYIK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 267 RWLQARGRIRFWKVRMRPGMPVLFGEAGRALVLGLPGNPVSVLATFHVFGRTLLDALQGrepRPCWRARL-----AAPWH 341
Cdd:PRK14491 453 TALAKLGQIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPALRKLAG---EQNWQPLLfpaiaDETLR 529
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 317465517 342 KRHDRLEFLRGRLDQDANATLCVHPEPADGSHRLRAAASSDVLIVLEDGANAYVAGDVVEVLPL 405
Cdd:PRK14491 530 SRQGRTEFSRGIYHLGADGRLHVRTTGKQGSGILSSMSEANCLIEIGPAAETVNAGETVTIQPL 593
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
32-172 |
1.33e-49 |
|
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of these contains the conserved DGXA motif. This region is found in proteins involved in biosynthesis of molybdopterin cofactor however the exact molecular function of this region is uncertain.
Pssm-ID: 460923 [Multi-domain] Cd Length: 147 Bit Score: 164.66 E-value: 1.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 32 VATRRADGRVLAADVVAPIPLPAFDNSAMDGFAVRHADLSAAAPVTLELAGEQFagpdlGLAVGPGQCVRITTGAPLPSG 111
Cdd:pfam03453 11 LEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNPIAAGEPP-----GPLLPGGEAVRIMTGAPLPEG 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 317465517 112 ADTIVIREDAIEQDGR-VQVPAGIRAGAHVRRQGEDVATGDVVLRAGQVLTPARIGLAAALG 172
Cdd:pfam03453 86 ADAVVMVEDTEEGGGRtVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
182-317 |
4.00e-33 |
|
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.
Pssm-ID: 272944 [Multi-domain] Cd Length: 148 Bit Score: 121.27 E-value: 4.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 182 PTVAVFASGDELAEPGMPLRPGQVYNSNREQLMAQLRDAGLEPVAWPTLPDDPVLIAAVLDDAVENFDLVLTCGAVSAGE 261
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 317465517 262 KDHLP--------RWLQARGRIR---FWKVRMRPGMPVLFGEAGRALVLGLPGNPVSVLATFHVFGR 317
Cdd:TIGR00177 81 RDVTPealeelgeKEIPGFGEFRmlsSLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLIL 147
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
185-315 |
5.21e-25 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 99.20 E-value: 5.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 185 AVFASGDELaepgmpLRPGQVYNSNREQLMAQLRDAGLEPVAWPTL--PDDPVLIAAVLDDAVENFDLVLTCGAVSAGEK 262
Cdd:smart00852 1 AIISTGDEL------LSGGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 317465517 263 DHLPRWLQARG--RIRFWKVRMRPGMP-----VLFGEAG----RALVLGLPGNPVSVLATFHVF 315
Cdd:smart00852 75 DLTPEALAELGgrELLGHGVAMRPGGPpgplaNLSGTAPgvrgKKPVFGLPGNPVAALVMFEEL 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
29-405 |
1.21e-166 |
|
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; Molybdopterin Mo-transferase (molybdopterin biosynthesis) is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440072 [Multi-domain] Cd Length: 401 Bit Score: 472.65 E-value: 1.21e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 29 TEQVATRRADGRVLAADVVAPIPLPAFDNSAMDGFAVRHADLSAAAPVTLELAGEQFAGPDLGLAVGPGQCVRITTGAPL 108
Cdd:COG0303 20 TETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVTLRVVGEIAAGSPPPGPLGPGEAVRIMTGAPL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 109 PSGADTIVIREDAIEQDGRVQVPAGIRAGAHVRRQGEDVATGDVVLRAGQVLTPARIGLAAALGIDRLEVAARPTVAVFA 188
Cdd:COG0303 100 PEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLLASLGIAEVPVYRRPRVAILS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 189 SGDELAEPGMPLRPGQVYNSNREQLMAQLRDAGLEPVAWPTLPDDPVLIAAVLDDAVENFDLVLTCGAVSAGEKDHLPRW 268
Cdd:COG0303 180 TGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEADLVITSGGVSVGDYDLVKEA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 269 LQARG-RIRFWKVRMRPGMPVLFGEAGRALVLGLPGNPVSVLATFHVFGRTLLDALQGRE--PRPCWRARLAAPWHKRHD 345
Cdd:COG0303 260 LEELGaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGLPppPPPRVRARLAEDLPKKPG 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 346 RLEFLRGRLDQDANaTLCVHPEPADGSHRLRAAASSDVLIVLEDGANAYVAGDVVEVLPL 405
Cdd:COG0303 340 RTEFLRVRLERDDG-ELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEVLLL 398
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
29-405 |
7.62e-159 |
|
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF), an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MoeA, together with MoaB, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes.
Pssm-ID: 238452 [Multi-domain] Cd Length: 394 Bit Score: 452.72 E-value: 7.62e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 29 TEQVATRRADGRVLAADVVAPIPLPAFDNSAMDGFAVRHADLsAAAPVTLELAGEQFAGPDLGLAVGPGQCVRITTGAPL 108
Cdd:cd00887 17 TETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADT-AGASVTLRVVGEIPAGEPPDGPLGPGEAVRIMTGAPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 109 PSGADTIVIREDAIEQDGRVQVPAGIRAGAHVRRQGEDVATGDVVLRAGQVLTPARIGLAAALGIDRLEVAARPTVAVFA 188
Cdd:cd00887 96 PEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAEVPVYRRPRVAIIS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 189 SGDELAEPGMPLRPGQVYNSNREQLMAQLRDAGLEPVAWPTLPDDPVLIAAVLDDAVENFDLVLTCGAVSAGEKDHLPR- 267
Cdd:cd00887 176 TGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGVSVGDYDFVKEv 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 268 WLQARGRIRFWKVRMRPGMPVLFGEAGRALVLGLPGNPVSVLATFHVFGRTLLDALQGRE--PRPCWRARLAAPWHKRHD 345
Cdd:cd00887 256 LEELGGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPepEPPRVKARLAEDLKSKPG 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 346 RLEFLRGRLDQDaNATLCVHPEPADGSHRLRAAASSDVLIVLEDGANAYVAGDVVEVLPL 405
Cdd:cd00887 336 RREFLRVRLERD-EGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLLL 394
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
29-405 |
1.41e-108 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 331.58 E-value: 1.41e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 29 TEQVATRRADGRVLAADVVAPIPLPAFDNSAMDGFAVRHADLSAA--APVTLELAGEQFAGPdlglaVGPGQCVRITTGA 106
Cdd:PRK14491 218 TEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPEsyTLVGEVLAGHQYDGT-----LQAGEAVRIMTGA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 107 PLPSGADTIVIREDAIEQDGRVQVPAGIRAGAHVRRQGEDVATGDVVLRAGQVLTPARIGLAAALGIDRLEVAARPTVAV 186
Cdd:PRK14491 293 PVPAGADTVVMRELATQDGDKVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPVFRRPKVAV 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 187 FASGDELAEPGMPLRPGQVYNSNREQLMAQLRDAGLEPVAWPTLPDDPVLIAAVLDDAVENFDLVLTCGAVSAGEKDHLP 266
Cdd:PRK14491 373 FSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISSGGVSVGDADYIK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 267 RWLQARGRIRFWKVRMRPGMPVLFGEAGRALVLGLPGNPVSVLATFHVFGRTLLDALQGrepRPCWRARL-----AAPWH 341
Cdd:PRK14491 453 TALAKLGQIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPALRKLAG---EQNWQPLLfpaiaDETLR 529
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 317465517 342 KRHDRLEFLRGRLDQDANATLCVHPEPADGSHRLRAAASSDVLIVLEDGANAYVAGDVVEVLPL 405
Cdd:PRK14491 530 SRQGRTEFSRGIYHLGADGRLHVRTTGKQGSGILSSMSEANCLIEIGPAAETVNAGETVTIQPL 593
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
29-351 |
4.07e-95 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 297.51 E-value: 4.07e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 29 TEQVATRRADGRVLAADVVAPIPLPAFDNSAMDGFAVRHADLSAA---APVTLELAGEQFAGPDLGLAVGPGQCVRITTG 105
Cdd:PRK14498 30 TEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGAseaNPVRLKLGGEVHAGEAPDVEVEPGEAVEIATG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 106 APLPSGADTIVIREDAIEQD-GRVQVPAGIRAGAHVRRQGEDVATGDVVLRAGQVLTPARIGLAAALGIDRLEVAARPTV 184
Cdd:PRK14498 110 APIPRGADAVVMVEDTEEVDdDTVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTPRDIGALAAGGVAEVPVYKKPRV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 185 AVFASGDELAEPGMPLRPGQVYNSNREQLMAQLRDAGLEPVAWPTLPDDPVLIAAVLDDAVENFDLVLTCGAVSAGEKDH 264
Cdd:PRK14498 190 GIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDLVLLSGGTSAGAGDV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 265 LPRWLQARGRIRFWKVRMRPGMPVLFGEAGRALVLGLPGNPVSVLATFHVFGRTLLDALQGREP--RPCWRARLAAPWHK 342
Cdd:PRK14498 270 TYRVIEELGEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVAPLLRKLAGLPPpeRATVKARLARRVRS 349
|
....*....
gi 317465517 343 RHDRLEFLR 351
Cdd:PRK14498 350 ELGREEFVP 358
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
29-404 |
4.63e-92 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 283.14 E-value: 4.63e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 29 TEQVATRRADGRVLAADVVAPIPLPAFDNSAMDGFAVRHADLSAAAPvtLELAGEQFAGPDLGLAVGPGQCVRITTGAPL 108
Cdd:PRK10680 27 TETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQP--LPVAGKAFAGQPFHGEWPAGTCIRIMTGAPV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 109 PSGADTIVIREDAIEQDGRVQVPAGIRAGAHVRRQGEDVATGDVVLRAGQVLTPARIGLAAALGIDRLEVAARPTVAVFA 188
Cdd:PRK10680 105 PEGCEAVVMQEQTEQTDDGVRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAELPVLASLGIAEVPVVRKVRVALFS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 189 SGDELAEPGMPLRPGQVYNSNREQLMAQLRDAGLEPVAWPTLPDDPVLIAAVLDDAVENFDLVLTCGAVSAGEKDHLPRW 268
Cdd:PRK10680 185 TGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEADSQADVVISSGGVSVGEADYTKTI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 269 LQARGRIRFWKVRMRPGMPVLFGEAGRALVLGLPGNPVSVLATFHVFGRTLLDALQGR---EPRPCWRARLAAPWHKRHD 345
Cdd:PRK10680 265 LEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSGNtasGLPPRQRVRTASRLKKTPG 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 317465517 346 RLEFLRGRLDQDANATLCVHPEPADGSHRLRAAASSDVLIVLEDGANAYVAGDVVEVLP 404
Cdd:PRK10680 345 RLDFQRGILQRNADGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNVEVGEWVEVEP 403
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
30-404 |
1.00e-65 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 215.17 E-value: 1.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 30 EQVATRRADGRVLAADVVAPIPLPAFDNSAMDGFAVRHADLSAAAPVTLElAGEQFAGPDLGLAVGPGQCVRITTGAPLP 109
Cdd:PRK14690 43 KELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQVLPLI-EGRAAAGVPFSGRVPEGMALRILTGAALP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 110 SGADTIVIREDAIEQDGRVQVPAGIRAGAHVRRQGEDVATGDVVLRAGQVLTPARIGLAAALGIDRLEVAARPTVAVFAS 189
Cdd:PRK14690 122 EGVDTVVLEEDVAGDGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRVSVRRPLRVAVLST 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 190 GDELAEPGMPLRPGQVYNSNREQLMAQLRDAGLEPVAWPTLPDDPVLIAAVLDDAVENFDLVLTCGAVSAGEKDHLPRWL 269
Cdd:PRK14690 202 GDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAEADVILTSGGASAGDEDHVSALL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 270 QARGRIRFWKVRMRPGMPVLFGEAGRALVLGLPGNPVSVLATFHVFGRTLLDALQGR---EPRPcWRARLAAPWHKRHDR 346
Cdd:PRK14690 282 REAGAMQSWRIALKPGRPLALGLWQGVPVFGLPGNPVAALVCTLVFARPAMSLLAGEgwsEPQG-FTVPAAFEKRKKPGR 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 317465517 347 LEFLRGRLDQDanatlCVHPEPADGSHRLRAAASSDVLIVLEDGANAYVAGDVVEVLP 404
Cdd:PRK14690 361 REYLRARLRQG-----HAEVFRSEGSGRISGLSWAEGLVELGDGARRIAPGDPVRFIP 413
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
37-403 |
4.41e-61 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 208.90 E-value: 4.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 37 ADGRVLAADVVAPIPLPAFDNSAMDGFAVRHADLSAAAPVTlelaGEQFAGPD-LGLAVGPGQCVRITTGAPLPSGADTI 115
Cdd:PLN02699 34 ALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVI----TESRAGNDgLGVTLTPGTVAYVTTGGPIPDGADAV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 116 VIREDA-IEQDG-----RVQVPAGIRAGAHVRRQGEDVATGDVVLRAGQVLTPARIGLAAALGIDRLEVAARPTVAVFAS 189
Cdd:PLN02699 110 VQVEDTeVVEDPldgskRVRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASEIGLLATVGVTMVKVYPRPTVAILST 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 190 GDELAEPGMP-LRPGQVYNSNREQLMAQLRDAGLEPVAWPTLPDDPVLIAAVLDDAVE-NFDLVLTCGAVSAGEKDHLPR 267
Cdd:PLN02699 190 GDELVEPTTGtLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDEAISsGVDILLTSGGVSMGDRDFVKP 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 268 WLQARGRIRFWKVRMRPGMPVLFGE---------AGRALVLGLPGNPVSVLATFHVFGRTLLDALQG-REPRPC-WRARL 336
Cdd:PLN02699 270 LLEKRGTVYFSKVLMKPGKPLTFAEidaksapsnSKKMLAFGLPGNPVSCLVCFNLFVVPAIRYLAGwSNPHLLrVQARL 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 317465517 337 AAPWHKRHDRLEFLRGRL-----DQDANATLCVHPEPADGSHRLRAAASSDVLIVLEDGANAYVAGDVVEVL 403
Cdd:PLN02699 350 REPIKLDPVRPEFHRAIIrwklnDGSGNPGFVAESTGHQMSSRLLSMKSANALLELPATGNVLSAGTSVSAI 421
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
29-312 |
3.29e-59 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 201.58 E-value: 3.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 29 TEQVATRRADGRVLAADVVAPIPLPAFDNSAMDGFAVRHAdlsaAAPVTLELAGEQFAGPDLGLAVGPGQCVRITTGAPL 108
Cdd:PRK14497 30 IVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSS----CTPGEFKVIDKIGIGEFKEIHIKECEAVEVDTGSMI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 109 PSGADTIVIREDAIEQDG-RVQVPAGIRAGAHVRRQGEDVATGDVVLRAGQVLTPARIGLAAALGIDRLEVAARPTVAVF 187
Cdd:PRK14497 106 PMGADAVIKVENTKVINGnFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASLGISSVKVYEKPKIYLI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 188 ASGDELAEPGMPLRPGQVYNSNREQLMAQLRDAGLEPVAWPTLPDDPVLIAAVLDDAVENFDLVLTCGAVSAGEKDHLPR 267
Cdd:PRK14497 186 ATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVADVLILTGGTSAGEKDFVHQ 265
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 317465517 268 WLQARGRIRFWKVRMRPGMPVLFGEAGRALVLGLPGNPVSVLATF 312
Cdd:PRK14497 266 AIRELGNIIVHGLKIKPGKPTILGIVDGKPVIGLPGNIVSTMVVL 310
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
32-172 |
1.33e-49 |
|
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of these contains the conserved DGXA motif. This region is found in proteins involved in biosynthesis of molybdopterin cofactor however the exact molecular function of this region is uncertain.
Pssm-ID: 460923 [Multi-domain] Cd Length: 147 Bit Score: 164.66 E-value: 1.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 32 VATRRADGRVLAADVVAPIPLPAFDNSAMDGFAVRHADLSAAAPVTLELAGEQFagpdlGLAVGPGQCVRITTGAPLPSG 111
Cdd:pfam03453 11 LEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNPIAAGEPP-----GPLLPGGEAVRIMTGAPLPEG 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 317465517 112 ADTIVIREDAIEQDGR-VQVPAGIRAGAHVRRQGEDVATGDVVLRAGQVLTPARIGLAAALG 172
Cdd:pfam03453 86 ADAVVMVEDTEEGGGRtVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
182-317 |
4.00e-33 |
|
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.
Pssm-ID: 272944 [Multi-domain] Cd Length: 148 Bit Score: 121.27 E-value: 4.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 182 PTVAVFASGDELAEPGMPLRPGQVYNSNREQLMAQLRDAGLEPVAWPTLPDDPVLIAAVLDDAVENFDLVLTCGAVSAGE 261
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 317465517 262 KDHLP--------RWLQARGRIR---FWKVRMRPGMPVLFGEAGRALVLGLPGNPVSVLATFHVFGR 317
Cdd:TIGR00177 81 RDVTPealeelgeKEIPGFGEFRmlsSLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLIL 147
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
185-322 |
2.67e-25 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 100.02 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 185 AVFASGDELAepgmplrPGQVYNSNREQLMAQLRDAGLEPVAWPTLPDDPVLIAAVLDDAVENFDLVLTCGAVSAGEKDH 264
Cdd:pfam00994 1 AIITTGDELL-------PGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 265 LPRWLQARGRIR-------FWKVRMRPGMPVLFG-----EAGRALVLGLPGNPVSVLATFHVFGRTLLDA 322
Cdd:pfam00994 74 TPEALAELGGRElpgfeelFRGVSLKPGKPVGTApgailSRAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
185-315 |
5.21e-25 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 99.20 E-value: 5.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 185 AVFASGDELaepgmpLRPGQVYNSNREQLMAQLRDAGLEPVAWPTL--PDDPVLIAAVLDDAVENFDLVLTCGAVSAGEK 262
Cdd:smart00852 1 AIISTGDEL------LSGGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 317465517 263 DHLPRWLQARG--RIRFWKVRMRPGMP-----VLFGEAG----RALVLGLPGNPVSVLATFHVF 315
Cdd:smart00852 75 DLTPEALAELGgrELLGHGVAMRPGGPpgplaNLSGTAPgvrgKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
184-315 |
5.54e-20 |
|
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. The domain is presumed to bind molybdopterin.
Pssm-ID: 238387 [Multi-domain] Cd Length: 133 Bit Score: 85.09 E-value: 5.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 184 VAVFASGDELAepgmplrPGQVYNSNREQLMAQLRDAGLEPVAWPTLPDDPVLIAAVLDDAVENFDLVLTCGAVSAGEKD 263
Cdd:cd00758 2 VAIVTVSDELS-------QGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRD 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 317465517 264 HLPRWLQARGRIRFWKVR--MRPGMPVLFGEAGRALVLGLPGNPVSVLATFHVF 315
Cdd:cd00758 75 VTPEALAELGEREAHGKGvaLAPGSRTAFGIIGKVLIINLPGSPKSALTTFEAL 128
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
333-405 |
7.92e-15 |
|
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis of molybdopterin cofactor however the exact molecular function of this domain is uncertain. The structure of this domain is known and forms an incomplete beta barrel.
Pssm-ID: 460924 [Multi-domain] Cd Length: 72 Bit Score: 68.79 E-value: 7.92e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 317465517 333 RARLAAPWHKRHDRLEFLRGRLDQDANATLcVHPEPADGSHRLRAAASSDVLIVLEDGANAYVAGDVVEVLPL 405
Cdd:pfam03454 1 KARLARDLKSDPGRREFVRVRLHEEDGRYY-AEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVILL 72
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
183-255 |
3.58e-05 |
|
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin.
Pssm-ID: 238450 [Multi-domain] Cd Length: 170 Bit Score: 44.01 E-value: 3.58e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 317465517 183 TVAVFASGDELAepgmplrPGQVYNSNREQLMAQLRDAGLEPVAWPTLPDDPVLIAAVLDDAVENFDLVLTCG 255
Cdd:cd00885 1 TAEIIAIGDELL-------SGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTG 66
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
49-405 |
3.28e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 42.94 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 49 PIPLP--AFDNSAMDGFAVRHADLSAAAPVTLELAGEQFAGPdLGLAVGPGQCVRITTGAPLPSGADTIVIREDAIEQDG 126
Cdd:COG3321 860 RVPLPtyPFQREDAAAALLAAALAAALAAAAALGALLLAALA-AALAAALLALAAAAAAALALAAAALAALLALVALAAA 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 127 RVQVPAGIRAGAHVRRQGEDVATGDVVLRAGQVLTPARIGLAAALGIDRLEVAARPTVAVFASGDELAEPGMPLRPGQVY 206
Cdd:COG3321 939 AAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAA 1018
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 207 NSNREQLMAQLRDAGLEPVAWPTLPDDPVLIAAVLDDAVENFDLVLTCGAVSAGEKDHLPRWLQARGRIRFWKVRMRPGM 286
Cdd:COG3321 1019 AALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALA 1098
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317465517 287 PVLFGEAGRALVLGLPGNPVSVLATFHVFGRTLLDALQGREPRPCWRARLAAPWHKRHDRLEFLRGRLDQDANATLCVHP 366
Cdd:COG3321 1099 LAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALA 1178
|
330 340 350
....*....|....*....|....*....|....*....
gi 317465517 367 EPADGSHRLRAAASSDVLIVLEDGANAYVAGDVVEVLPL 405
Cdd:COG3321 1179 LALAAALAAALAGLAALLLAALLAALLAALLALALAALA 1217
|
|
| |
